Matches in SemOpenAlex for { <https://semopenalex.org/work/W1992377095> ?p ?o ?g. }
Showing items 1 to 85 of
85
with 100 items per page.
- W1992377095 endingPage "552" @default.
- W1992377095 startingPage "549" @default.
- W1992377095 abstract "The regulatory domain (RD) of the cystic fibrosis transmembrane conductance regulator (CFTR), the defective protein in cystic fibrosis, is the region of the channel that regulates the CFTR activity with multiple phosphorylation sites. This domain is an intrinsically disordered protein, characterized by lack of stable or unique tertiary structure. The disordered character of a protein is directly correlated with its function. The flexibility of RD may be important for its regulatory role: the continuous conformational change may be necessary for the progressive phosphorylation, and thus activation, of the channel. However, the lack of a defined and stable structure results in a considerable limitation when trying to in build a unique molecular model for the RD. Moreover, several evidences indicate significant structural differences between the native, non-phosphorylated state, and the multiple phosphorylated state of the protein. The aim of our work is to provide data to describe the conformations and the thermodynamic properties in these two functional states of RD. We have done the circular dichroism (CD) spectra in samples with a different degree of phosphorylation, from the non-phosphorylated state to a bona fide completely phosphorylated state. Analysis of CD spectra showed that the random coil and β-sheets secondary structure decreased with the polypeptide phosphorylation, at expenses of an increase of α-helix. This observation lead to interpret phosphorylation as a mechanism favoring a more structured state. We also studied the thermal denaturation curves of the protein in the two conditions, monitoring the changes of the mean residue ellipticity measured at 222 nm as a function of temperature, between 20 and 95 °C. The thermodynamic analysis of the denaturation curves shows that phosphorylation of the protein induces a state of lower stability of R domain, characterized by a lower transition temperature, and by a smaller Gibbs free energy difference between the native and the unfolded states." @default.
- W1992377095 created "2016-06-24" @default.
- W1992377095 creator A5018839622 @default.
- W1992377095 creator A5029781471 @default.
- W1992377095 creator A5079336753 @default.
- W1992377095 date "2012-07-01" @default.
- W1992377095 modified "2023-09-27" @default.
- W1992377095 title "Thermodynamic study of the native and phosphorylated regulatory domain of the CFTR" @default.
- W1992377095 cites W1617965928 @default.
- W1992377095 cites W1745204207 @default.
- W1992377095 cites W1966528069 @default.
- W1992377095 cites W1983581547 @default.
- W1992377095 cites W1989009320 @default.
- W1992377095 cites W2001758114 @default.
- W1992377095 cites W2026727321 @default.
- W1992377095 cites W2039413420 @default.
- W1992377095 cites W2058530636 @default.
- W1992377095 cites W2092468755 @default.
- W1992377095 cites W2156771958 @default.
- W1992377095 doi "https://doi.org/10.1016/j.bbrc.2012.05.165" @default.
- W1992377095 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22683332" @default.
- W1992377095 hasPublicationYear "2012" @default.
- W1992377095 type Work @default.
- W1992377095 sameAs 1992377095 @default.
- W1992377095 citedByCount "8" @default.
- W1992377095 countsByYear W19923770952012 @default.
- W1992377095 countsByYear W19923770952013 @default.
- W1992377095 countsByYear W19923770952014 @default.
- W1992377095 countsByYear W19923770952016 @default.
- W1992377095 countsByYear W19923770952021 @default.
- W1992377095 crossrefType "journal-article" @default.
- W1992377095 hasAuthorship W1992377095A5018839622 @default.
- W1992377095 hasAuthorship W1992377095A5029781471 @default.
- W1992377095 hasAuthorship W1992377095A5079336753 @default.
- W1992377095 hasConcept C104317684 @default.
- W1992377095 hasConcept C11960822 @default.
- W1992377095 hasConcept C12554922 @default.
- W1992377095 hasConcept C133571119 @default.
- W1992377095 hasConcept C185592680 @default.
- W1992377095 hasConcept C2778428886 @default.
- W1992377095 hasConcept C2778815515 @default.
- W1992377095 hasConcept C34349673 @default.
- W1992377095 hasConcept C55493867 @default.
- W1992377095 hasConcept C62614982 @default.
- W1992377095 hasConcept C75599170 @default.
- W1992377095 hasConcept C86803240 @default.
- W1992377095 hasConcept C87325107 @default.
- W1992377095 hasConcept C97029542 @default.
- W1992377095 hasConceptScore W1992377095C104317684 @default.
- W1992377095 hasConceptScore W1992377095C11960822 @default.
- W1992377095 hasConceptScore W1992377095C12554922 @default.
- W1992377095 hasConceptScore W1992377095C133571119 @default.
- W1992377095 hasConceptScore W1992377095C185592680 @default.
- W1992377095 hasConceptScore W1992377095C2778428886 @default.
- W1992377095 hasConceptScore W1992377095C2778815515 @default.
- W1992377095 hasConceptScore W1992377095C34349673 @default.
- W1992377095 hasConceptScore W1992377095C55493867 @default.
- W1992377095 hasConceptScore W1992377095C62614982 @default.
- W1992377095 hasConceptScore W1992377095C75599170 @default.
- W1992377095 hasConceptScore W1992377095C86803240 @default.
- W1992377095 hasConceptScore W1992377095C87325107 @default.
- W1992377095 hasConceptScore W1992377095C97029542 @default.
- W1992377095 hasFunder F4320325077 @default.
- W1992377095 hasIssue "3" @default.
- W1992377095 hasLocation W19923770951 @default.
- W1992377095 hasLocation W19923770952 @default.
- W1992377095 hasOpenAccess W1992377095 @default.
- W1992377095 hasPrimaryLocation W19923770951 @default.
- W1992377095 hasRelatedWork W1992377095 @default.
- W1992377095 hasRelatedWork W1996911561 @default.
- W1992377095 hasRelatedWork W2046395359 @default.
- W1992377095 hasRelatedWork W2059266343 @default.
- W1992377095 hasRelatedWork W2079330719 @default.
- W1992377095 hasRelatedWork W2416801748 @default.
- W1992377095 hasRelatedWork W2469707425 @default.
- W1992377095 hasRelatedWork W2548903987 @default.
- W1992377095 hasRelatedWork W3155603390 @default.
- W1992377095 hasRelatedWork W4322012258 @default.
- W1992377095 hasVolume "423" @default.
- W1992377095 isParatext "false" @default.
- W1992377095 isRetracted "false" @default.
- W1992377095 magId "1992377095" @default.
- W1992377095 workType "article" @default.